{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Harikumar KG"],"funding":["NIGMS NIH HHS"],"pagination":["4390"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11116414"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Class B G protein-coupled receptors can form dimeric complexes important for high potency biological effects. Here, we apply pharmacological, biochemical, and biophysical techniques to cells and membranes expressing the prototypic secretin receptor (SecR) to gain insights into secretin binding to homo-dimeric and monomeric SecR. Spatial proximity between peptide and receptor residues, probed by disulfide bond formation, demonstrates that the secretin N-terminus moves from adjacent to extracellular loop 3 (ECL3) at wild type SecR toward ECL2 in non-dimerizing mutants. Analysis of fluorescent secretin analogs demonstrates stable engagement of the secretin C-terminal region within the receptor extracellular domain (ECD) for both dimeric and monomeric receptors, while the mid-region exhibits l"],"journal":["Nature communications"],"pubmed_title":["Impact of secretin receptor homo-dimerization on natural ligand binding."],"pmcid":["PMC11116414"],"funding_grant_id":["R01 GM132095"],"pubmed_authors":["Sexton PM","Miller LJ","Wootten D","Piper SJ","Christopoulos A","Harikumar KG"],"additional_accession":[]},"is_claimable":false,"name":"Impact of secretin receptor homo-dimerization on natural ligand binding.","description":"Class B G protein-coupled receptors can form dimeric complexes important for high potency biological effects. Here, we apply pharmacological, biochemical, and biophysical techniques to cells and membranes expressing the prototypic secretin receptor (SecR) to gain insights into secretin binding to homo-dimeric and monomeric SecR. Spatial proximity between peptide and receptor residues, probed by disulfide bond formation, demonstrates that the secretin N-terminus moves from adjacent to extracellular loop 3 (ECL3) at wild type SecR toward ECL2 in non-dimerizing mutants. Analysis of fluorescent secretin analogs demonstrates stable engagement of the secretin C-terminal region within the receptor extracellular domain (ECD) for both dimeric and monomeric receptors, while the mid-region exhibits l","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T19:58:51.592Z","creation":"2026-04-19T03:14:01.199Z"},"accession":"S-EPMC11116414","cross_references":{"pubmed":["38782989"],"doi":["10.1038/s41467-024-48853-6"]}}